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Relevant bibliographies by topics / Cationic antimicrobial peptides

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Academic literature on the topic 'Cationic antimicrobial peptides'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Cationic antimicrobial peptides"

1

Bradshaw, Jeremy P. "Cationic Antimicrobial Peptides." BioDrugs 17, no. 4 (2003): 233–40. http://dx.doi.org/10.2165/00063030-200317040-00002.

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Ball, S. L., G. P. Siou, J. A. Wilson, A. Howard, B. H. Hirst, and J. Hall. "Expression and immunolocalisation of antimicrobial peptides within human palatine tonsils." Journal of Laryngology & Otology 121, no. 10 (2007): 973–78. http://dx.doi.org/10.1017/s0022215107006184.

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Background: Recurrent acute tonsillitis is one of the most frequent ENT referrals, yet its pathogenesis remains poorly understood, and tonsillectomy still costs the National Health Service more than £60 000 000 annually. Antimicrobial cationic peptides are components of the innate immune system. They are generally small, highly positively charged peptides with broad spectrum antimicrobial activity which function as the body's ‘natural antibiotics'. The role of antimicrobial cationic peptides in the susceptibility of patients to recurrent acute tonsillitis is unknown.Aims: To characterise and c

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Stark, Margareta, Li-Ping Liu, and Charles M. Deber. "Cationic Hydrophobic Peptides with Antimicrobial Activity." Antimicrobial Agents and Chemotherapy 46, no. 11 (2002): 3585–90. http://dx.doi.org/10.1128/aac.46.11.3585-3590.2002.

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ABSTRACT The MICs of cationic, hydrophobic peptides of the prototypic sequence KKAAAXAAAAAXAAWAAXAAAKKKK-amide (where X is one of the 20 commonly occurring amino acids) are in a low micromolar range for a panel of gram-negative and gram-positive bacteria, with no or low hemolytic activity against human and rabbit erythrocytes. The peptides are active only when the average segmental hydrophobicity of the 19-residue core is above an experimentally determined threshold value (where X is Phe, Trp, Leu, Ile, Met, Val, Cys, or Ala). Antimicrobial activity could be increased by using peptides that we

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4

Bechinger, B., and S. U. Gorr. "Antimicrobial Peptides: Mechanisms of Action and Resistance." Journal of Dental Research 96, no. 3 (2016): 254–60. http://dx.doi.org/10.1177/0022034516679973.

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More than 40 antimicrobial peptides and proteins (AMPs) are expressed in the oral cavity. These AMPs have been organized into 6 functional groups, 1 of which, cationic AMPs, has received extensive attention in recent years for their promise as potential antibiotics. The goal of this review is to describe recent advances in our understanding of the diverse mechanisms of action of cationic AMPs and the bacterial resistance against these peptides. The recently developed peptide GL13K is used as an example to illustrate many of the discussed concepts. Cationic AMPs typically exhibit an amphipathic

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Friedrich, Carol, Monisha G. Scott, Nedra Karunaratne, Hong Yan, and Robert E. W. Hancock. "Salt-Resistant Alpha-Helical Cationic Antimicrobial Peptides." Antimicrobial Agents and Chemotherapy 43, no. 7 (1999): 1542–48. http://dx.doi.org/10.1128/aac.43.7.1542.

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ABSTRACT Analogues based on the insect cecropin–bee melittin hybrid peptide (CEME) were studied and analyzed for activity and salt resistance. The new variants were designed to have an increase in amphipathic α-helical content (CP29 and CP26) and in overall positive charge (CP26). The α-helicity of these peptides was demonstrated by circular dichroism spectroscopy in the presence of liposomes. CP29 was shown to have activity against gram-negative bacteria that was similar to or better than those of the parent peptides, and CP26 had similar activity. CP29 had cytoplasmic membrane permeabilizati

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Zhang, Lijuan, and Timothy J. Falla. "Cationic antimicrobial peptides – an update." Expert Opinion on Investigational Drugs 13, no. 2 (2004): 97–106. http://dx.doi.org/10.1517/13543784.13.2.97.

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Brown, Kelly L., and Robert EW Hancock. "Cationic host defense (antimicrobial) peptides." Current Opinion in Immunology 18, no. 1 (2006): 24–30. http://dx.doi.org/10.1016/j.coi.2005.11.004.

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Ciumac, Daniela, Haoning Gong, Xuzhi Hu, and Jian Ren Lu. "Membrane targeting cationic antimicrobial peptides." Journal of Colloid and Interface Science 537 (March 2019): 163–85. http://dx.doi.org/10.1016/j.jcis.2018.10.103.

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Frecer, V., B. Ho, and J. L. Ding. "De Novo Design of Potent Antimicrobial Peptides." Antimicrobial Agents and Chemotherapy 48, no. 9 (2004): 3349–57. http://dx.doi.org/10.1128/aac.48.9.3349-3357.2004.

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ABSTRACT Lipopolysaccharide (LPS), shed by gram-negative bacteria during infection and antimicrobial therapy, may lead to lethal endotoxic shock syndrome. A rational design strategy based on the presumed mechanism of antibacterial effect was adopted to design cationic antimicrobial peptides capable of binding to LPS through tandemly repeated sequences of alternating cationic and nonpolar residues. The peptides were designed to achieve enhanced antimicrobial potency due to initial bacterial membrane binding with a reduced risk of endotoxic shock. The peptides designed displayed binding affiniti

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Walkenhorst, William F., J. Wolfgang Klein, Phuong Vo, and William C. Wimley. "pH Dependence of Microbe Sterilization by Cationic Antimicrobial Peptides." Antimicrobial Agents and Chemotherapy 57, no. 7 (2013): 3312–20. http://dx.doi.org/10.1128/aac.00063-13.

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ABSTRACTWe recently described a family of cationic antimicrobial peptides (CAMPs) selected from a combinatorial library that exhibited potent, broad-spectrum activity at neutral pH and low ionic strength. To further delimit the utility and activity profiles of these peptides, we investigated the effects of solution conditions, such as pH and ionic strength, on the efficacy of the peptide antimicrobials against a panel of microorganisms. Peptide minimum sterilizing concentrations (MSCs) varied linearly with pH for each subtype within our family of CAMPs for all organisms tested. The peptides we

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Dissertations / Theses on the topic "Cationic antimicrobial peptides"

1

Termén, Stefan. "Expression of cathelicidin antimicrobial peptides in man and rat /." Stockholm, 2004. http://diss.kib.ki.se/2004/91-7140-138-5/.

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Shyam, Radhe. "Cationic amphipathic peptoid oligomers as antimicrobial peptide mimics." Thesis, Université Clermont Auvergne‎ (2017-2020), 2018. http://www.theses.fr/2018CLFAC048/document.

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Les organismes vivants produisent des peptides antimicrobiens (PAMs) pour se protéger contre les microbes. La résistance croissante aux antibiotiques nécessite le développement de nouvelles stratégies thérapeutiques et les PAMs sont des candidats prometteurs pour résoudre ce problème. Ils possèdent une activité à large spectre et leur principal mécanisme d'action par perméation de la membrane engendre peu de phénomènes de résistance. Néanmoins, leur faible biodisponibilité empêche leur utilisation. Certaines limitations peuvent être surmontées en développant des mîmes de PAMs qui conservent le

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Harris, Mark R. "Effects of cationic antimicrobial peptides on Candida and Saccharomyces species." Thesis, St Andrews, 2010. http://hdl.handle.net/10023/881.

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Findlay, Brandon. "Design and synthesis of cationic amphiphiles." American Society for Microbiology, 2010. http://hdl.handle.net/1993/21708.

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Cationic antimicrobial peptides (CAMPs) are produced by plants, animals and bacteria to protect their host against antagonistic microbes. The antitheses of selective antibiotics, these peptides are drawn by electrostatic and hydrophobic interactions to targets as diverse as the bacterial membrane, nucleic acids and serum proteins. This lack of specificity is their greatest strength, as mutations to single genes rarely lead to bacterial resistance. Resistance may be conferred by large scale alterations in cell envelope composition, which generally reduces bacterial fitness in the absence of

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Bagheri, Mojtaba [Verfasser]. "Cationic antimicrobial peptides : thermodynamic characterization of peptide-lipid interactions and biological efficacy of surface-tethered peptides / Mojtaba Bagheri." Berlin : Freie Universität Berlin, 2010. http://d-nb.info/1025126971/34.

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Cheng, John Tien Jui. "Investigating the structure-function relationship of cationic antimicrobial peptides and lipopeptides." Thesis, University of British Columbia, 2010. http://hdl.handle.net/2429/29358.

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Antibiotics have been playing a major role in combating bacterial infections for centuries. Since the discovery of modern antibiotics, numerous derivatives have been designed and developed to treat different bacterial infections. Recently, antibiotic resistance has been continuously and increasingly reported. The lack of antibiotic alternatives makes these resistant bacteria become more difficult to eliminate. Antimicrobial peptides constitute a major part of the innate immune system of an organism. Their high activity and little resistance make them ideal candidates for novel antibiotic

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Tollin, Maria. "Antimicrobial peptides and proteins in innate immunity : emphasis on isolation, characterization and gene regulation /." Stockholm, 2005. http://diss.kib.ki.se/2005/91-7140-270-5/.

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Miskimins, Mills Beth Ellen. "Modulatory activities of glycosaminoglycans and other polyanionic polysaccharides on cationic antimicrobial peptides." Diss., University of Iowa, 2010. https://ir.uiowa.edu/etd/557.

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Cationic antimicrobial peptides (CAPs) are an important component of the innate immune system and are instrumental in the elimination of bacteria, viruses, protozoa, yeast, fungi and cancerous cells from the body. CAPs are comprised of less than 100 amino acids and have a net positive charge due to a multitude of basic residues in their primary sequences. CAPs exert their antimicrobial activity primarily through the formation of pores in microbial membranes, but also play important immunostimulatory roles in the body. Glycosaminoglycans (GAGs) are negatively charged, polydisperse linear polysa

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Bergman, Peter. "Antimicrobial peptides and pathogenic Neisseria : experimental studies in mouse, man and rat /." Stockholm, 2005. http://diss.kib.ki.se/2005/91-7140-428-7/.

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Lisanby, Mark W. "Examination of the capacity of cathelicidins to control Bacillus anthracis pathogenesis." Thesis, Birmingham, Ala. : University of Alabama at Birmingham, 2009. https://www.mhsl.uab.edu/dt/2009p/lisanby.pdf.

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Books on the topic "Cationic antimicrobial peptides"

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Antimicrobial peptides: Methods and protocols. Humana Press/Springer, 2010.

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Drider, Djamel, and Sylvie Rebuffat. Prokaryotic antimicrobial peptides: From genes to applications. Springer Verlag, 2011.

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Rajasekaran, K. Small wonders: Peptides for disease control. Edited by American Chemical Society. Division of Agricultural and Food Chemistry. American Chemical Society, 2012.

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Antimicrobial Peptides And Innate Immunity. Springer, 2013.

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Hiemstra, Pieter S., and Sebastian A. J. Zaat. Antimicrobial Peptides and Innate Immunity. Springer, 2015.

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Hiemstra, Pieter S., and Sebastian A. J. Zaat. Antimicrobial Peptides and Innate Immunity. Springer, 2013.

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Drider, Djamel, and Sylvie Rebuffat. Prokaryotic Antimicrobial Peptides: From Genes to Applications. Springer, 2011.

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Drider, Djamel, and Sylvie Rebuffat. Prokaryotic Antimicrobial Peptides: From Genes to Applications. Springer, 2014.

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Kuo, Hsin Hen. Alginate in Pseudomonas aeruginosa biofilms: Barrier to cationic antimicrobial peptides. 2007.

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Antimicrobial Peptides Discovery Design And Novel Therapeutic Strategies. CABI Publishing, 2010.

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Book chapters on the topic "Cationic antimicrobial peptides"

1

Cole, Alexander M., and Amy Liese Cole. "Dichotomous Roles of Cationic Polypeptides Targeting HIV." In Antimicrobial Peptides. Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24199-9_8.

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Goytia, Maira, Justin L. Kandler, and William M. Shafer. "Mechanisms and Significance of Bacterial Resistance to Human Cationic Antimicrobial Peptides." In Antimicrobial Peptides and Innate Immunity. Springer Basel, 2012. http://dx.doi.org/10.1007/978-3-0348-0541-4_9.

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Robey, Marianne, William O'Connell, and Nicholas P. Cianciotto. "Resistance of Legionella pneumophila to Cationic Antimicrobial Peptides." In Legionella. ASM Press, 2014. http://dx.doi.org/10.1128/9781555817985.ch7.

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Hilpert, Kai, Christopher D. Fjell, and Artem Cherkasov. "Short Linear Cationic Antimicrobial Peptides: Screening, Optimizing, and Prediction." In Peptide-Based Drug Design. Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-419-3_8.

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Sánchez-Gómez, Susana, Guillermo MartÍnez de Tejada, José Leiva-Leon, et al. "Comparing Antimicrobial and Membrane Permeabilizing Activity of Peptides Derived from Human Cationic Proteins." In Understanding Biology Using Peptides. Springer New York, 2006. http://dx.doi.org/10.1007/978-0-387-26575-9_104.

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Blazyk, Jack, Janet Hammer, Yi Jin, Yu Zhang, and Fang Zhu. "Relationship Between Amphipathic Secondary Structure and Activity in Model Linear Cationic Antimicrobial Peptides." In Peptides: The Wave of the Future. Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-010-0464-0_221.

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Pate, Michelle, and Jack Blazyk. "Methods for Assessing the Structure and Function of Cationic Antimicrobial Peptides." In Methods In Molecular Medicine™. Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-246-5_13.

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Hilchie, Ashley L., Melanie R. Power Coombs, and David W. Hoskin. "Obstacles and Solutions to the Use of Cationic Antimicrobial Peptides in the Treatment of Cancer." In ACS Symposium Series. American Chemical Society, 2012. http://dx.doi.org/10.1021/bk-2012-1095.ch004.

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Aisenbrey, Christopher, Arnaud Marquette, and Burkhard Bechinger. "The Mechanisms of Action of Cationic Antimicrobial Peptides Refined by Novel Concepts from Biophysical Investigations." In Advances in Experimental Medicine and Biology. Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-13-3588-4_4.

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Jiang, Ziqing, Adriana I. Vasil, John Hale, Robert E. W. Hancock, Michael L. Vasil, and Robert S. Hodges. "Effects of net charge and the number of positively charged residues on the biological activity of amphipathic α-helical cationic antimicrobial peptides." In Advances in Experimental Medicine and Biology. Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-73657-0_246.

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Conference papers on the topic "Cationic antimicrobial peptides"

1

Pulido, D., M. Torrent, M. V. Nogués, and E. Boix. "The role of Gram-negative envelope LPS on the bactericidal properties of proteins and peptides: the case of eosinophil cationic protein." In Proceedings of the International Conference on Antimicrobial Research (ICAR2010). WORLD SCIENTIFIC, 2011. http://dx.doi.org/10.1142/9789814354868_0008.

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